Proteolytic degradation of the flavonoid regulators, TRANSPARENT TESTA8 and TRANSPARENT TESTA GLABRA1, in Arabidopsis is mediated by the ubiquitin/26sproteasome system

Barunava Patra, Sitakanta Pattanaik, Ling Yuan

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Regulated proteolysis by the ubiquitin/26S proteasome system (uPS) has emerged as a major posttranslational control mechanism regulating transcription factor (tF) activity in plants. anthocyanin biosynthesis in Arabidopsis is regulated by a ternary complex comprised of basic helix-loop-helix (bhLh), r2r3mYB and WD-repeat (WDr) proteins. the bhLh TF, TRANSPARENT TESTA 8 (tt8), and the WDr protein, tranSParEnt tESta GLaBra1 (ttG1), are essential for expression of late flavonoid biosynthesis genes. Previous studies have demonstrated that the turnover of several anthocyanin pathway regulators is controlled by the uPS. here, we show that tt8 and ttG1 are short-lived and targeted by the uPS for degradation. our findings further extend our understanding of the role of the uPS in the regulation of anthocyanin biosynthesis in plants.

Original languageEnglish
JournalPlant Signaling and Behavior
Volume8
Issue number10
DOIs
StatePublished - Oct 2013

Bibliographical note

Funding Information:
This work is supported by a grant from the Kentucky Tobacco Research and Development Center (to LY). We thank KA Shen for critical comments of the manuscript.

Funding

This work is supported by a grant from the Kentucky Tobacco Research and Development Center (to LY). We thank KA Shen for critical comments of the manuscript.

FundersFunder number
The Kentucky Tobacco Research and Development Center

    Keywords

    • 26S proteasome
    • Anthocyanins
    • Flavonoids
    • TT8
    • TTG1

    ASJC Scopus subject areas

    • Plant Science

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